Results 171 to 180 of about 18,813 (211)

Hsp27 is persistently expressed in zebrafish skeletal and cardiac muscle tissues but dispensable for their morphogenesis

open access: yesCell Stress and Chaperones, 2009
Constitutive expression of Hsp27 has been demonstrated in vertebrate embryos, especially in developing skeletal and cardiac muscle. Results of several previous studies have indicated that Hsp27 could play a role in the development of these tissues.
Michael E Konkel   +2 more
exaly   +2 more sources

Hsp27 as a Therapeutic Target in Cancers

Current Drug Targets, 2014
Heat shock protein 27 (Hsp27), induced by heat shock, environmental and pathophysiological stressors, is a multidimensional protein that acts as a protein chaperone and an antioxidant. This protein plays a major role in the inhibition of apoptosis and actin cytoskeletal remodeling.
Julie, Acunzo   +4 more
openaire   +2 more sources

Biological Significance of Decreased HSP27 in Human Atherosclerosis [PDF]

open access: yesArteriosclerosis, Thrombosis, and Vascular Biology, 2006
Objective— Because culprit atherosclerotic plaques contain proteases, we hypothesized that the diminished heat shock protein 27 (HSP27) released by atherosclerotic plaques could be due to proteolysis. We assessed the role of HSP27 in human vascular smooth muscle cells (VSMCs) under proteolytic injury.
Jean-Baptiste Michel   +2 more
exaly   +3 more sources

The Interaction of HSP27 with Daxx Identifies a Potential Regulatory Role of HSP27 in Fas‐Induced Apoptosis

Annals of the New York Academy of Sciences, 2000
Abstract: The heat shock protein HSP27 protects cells against a wide variety of toxic treatments and blocks apoptosis induced by exposures to anticancer drugs and activation of the death receptor fas. The molecular mechanisms of protection are unknown but appear to be regulated by phosphorylation of HSP27.
S J, Charette, J, Landry
openaire   +2 more sources

Constitutive expression of Hsp27 in the rat cochlea

Hearing Research, 2002
Heat shock protein-27 (Hsp27) is known to function as both a stress-inducible molecular chaperone and regulator of actin polymerization. For many cells in the cochlea, actin is part of the cytoskeleton and plays an important role in the maintenance of cochlear function.
Elena V, Leonova   +3 more
openaire   +2 more sources

Hsp27 as a Prognostic and Predictive Factor in Cancer

2002
Once the diagnosis of a particular type of cancer has been established, the physicians need to know the aggressiveness of the tumor in order to decide which treatments should be applied. The aggressiveness of the malignant tumor is evaluated by the clinic (e.g., growth rate or given symptoms), by laboratory/image data (e.g., presence of tumor markers ...
Daniel R, Ciocca, Laura M, Vargas-Roig
openaire   +2 more sources

Mammalian Hsp27

1997
Abstract Hsp25, Hsp28, mammalian small or low-molecular-weight heat shock protein (Arrigo, Landry, 1994). The nucleotide sequences of mammalian hsp27 genes encode proteins with highly conserved sequences. Hsp27.
openaire   +1 more source

Identification of a Site of Hsp27 Binding with Hsp27 and αB-Crystallin as Indicated by the Yeast Two-Hybrid System

Biochemical and Biophysical Research Communications, 1999
The small heat-shock proteins (sHsp), including Hsp27 and alphaB-crystallin, usually form large oligomers in cells. It has been suggested that the sHsp form oligomers by binding either a conserved C-terminal amino acid sequence or the less conserved N-terminal region. However, the site of binding has not been precisely determined. We used the yeast two-
C, Liu, M J, Welsh
openaire   +2 more sources

Structure–Functions of HspB1 (Hsp27)

2011
Human HspB1 (also denoted Hsp27) is a well-known member, together with alphaB-crystallin, of the small heat-shock (or stress) proteins (sHsps) (20-40 kDa). In this chapter, I describe procedures for testing the oligomeric and phosphorylation patterns of HspB1 as well as its interaction with specific partner/client polypeptides using tissue culture ...
openaire   +2 more sources

Role of Hsp27 and Related Proteins

1999
Investigations of the cellular response to thermal and other types of stresses have allowed the identification of families of proteins (the heat shock or stress proteins, Hsp) whose expression is enhanced when environmental conditions become deleterious (reviewed in Georgopoulos and Welch 1993; Morimoto et al. 1994).
A.-P. Arrigo, X. Préville
openaire   +1 more source

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